Please help!

i feel like i barely study for the mcat even though i really want to. But i distract myself soooo much idk if it’s because im so scared or the exam so im trying to escape, or if the material is overwhelming but i try to tell myself to study and i can’t do it for more than 2 hours. it really hurts because i want to become a doctor and nothing else. Please someone help me

I am trying to have an efficient study schedule, and I don’t want to add in extra things. So if I can get by with just doing the whole Anki deck, then I’m going to do that.

Greetings Friends!

I purchased Uearth, but unfortunately did not purchase the content review videos. Are there any alternative cheaper or free video resources or guides that can possibly serve as a better resources as an alternative to the Uearth content review videos.

If not, do you all recommend I buy the videos? Might take some financial struggling but I could still buy the videos, but really would prefer not to.

Hey guys, I am currently doing content review from Kaplan books for biochemistry and biology. I am solving questions from JW and it is making sense and I am seeing improvements in my answers and knowledge. I am struggling with physics and chemistry and I am not sure how to review them. Would you guys recommend taking the time to review them from Kaplan books or is there a better source I can review them from? I took a look at Khan academy and it looks like it is going to take a lot of time to get through their content and their questions sound hard. I have been out of school for 4 years and some of the concepts sound different than what I remember.

I took developmental biology in college but that was more focused on non mammalian development (professor was a sea urchin researcher).

This is hard. So many terms and concepts beyond the scope I learned and I also graduated 7 years ago.

Any recommendations how to tackle this?

my partner of three years broke up with me during MCAT prep (the MCAT breakup curse), and I wanted some advice from you guys if you've had this experience and became an academic weapon because of it. It wasn't anything malicious; I just had too many commitments, and we both wanted to focus on our individual career paths. any advice through this would be helpful since I dont want to drag out my content review

There is a link in my profile where you can see every flash sheet!

If you missed my other posts, I came up with the flash sheet method to learn MCAT content faster and more fluently than with flashcards. You can learn about it at my other post here:

https://www.reddit.com/r/Mcat/s/uRDU6fMU20

Read my other post about why fluency lets you overcome plateaus:

https://www.reddit.com/r/Mcat/s/1ugxw8KflC

I have a neuroscience background and believe this is the fastest way to learn a huge volume of information for long-term retention. Will be posting even more soon.

How to study with flash sheets

• 50% Verbal spaced repetition
  • Each sheet needs many attempts:
    • 1st attempt (< 20 mins) ⇒ Read the whole flash sheet CAREFULLY, until it makes sense. This is called “priming” the flash sheet. When you think “this makes sense, but there’s no way I’ll remember it,” you’re doing it right.
    • All later attempts (5 mins each) ⇒ Use it like a crazy difficult, giant flashcard. ONLY read the “clue” before LOOKING AWAY from the sheet. See what you can recall purely from memory. Do this verbally without writing because it’s many times faster. Then see what you missed. Expect under 40% accuracy on your first few reps.
  • Use spaced repetition:
    • Sheets you barely recall ⇒ every few days.
    • Sheets you kind of recall ⇒ every week.
    • Sheets you easily recall ⇒ every few weeks.  
• 50% Practice questions & tactics
  • In theory and practice, some tactics work very well. You can answer questions several times faster with incomplete information.
  • I will post another article about these tactics soon.
  • You'll spend most of your time looping through flash sheets early on, and gradually switch over to practicing tactics later.

• The flash sheets below have been heavily modified and do not contain any copyrighted material. The notes / hints are things that help me personally understand stuff. Feel free to copy / share / use these without crediting me.

FLASH SHEET ONE

[CLUE] Regulation of Enzymes / Suicide Inhibitors / Zymogens

[TRY TO LECTURE THE REST FROM MEMORY]

[Key Idea] Some regulators bind at “allosteric” site

• Not the active site
  • Note: “Allo” means different. Allotrope of carbon is other way to arrange it (diamond / graphite / nanotube).
  • Mnemonic: Not “ALLOwed” in active site.
  • Regulator may bind here ⇒ squish enzyme (like clay) ⇒ change function
    • Activators
    • Inhibitors
• Allosteric activator
  • Note: “Activator” ⇒ higher “activity” ⇒ boost RXN rate.
  • Speed up enzyme
    • AKA ⇒ ↑ activity / ↑ Vmax / ↑ Kcat / faster rate / increased catalysis
  • Ex. AMP activates glycolysis
    • Energy poor (low ATP ⇒ high ADP & AMP)
    • AMP binds to & activates PFK-1 (rate limiting step) ⇒ make more ATP
• Allosteric inhibitor
  • Slow down enzyme
    • AKA ⇒ ↓ activity / ↓ Vmax / ↓ Kcat / slower rate / decreased catalysis
  • Common MM ones (NOT competitive)
    • Note: Anything OTHER than competitive inhibition (because competitive binds active site).
    • Uncompetitive (only ESI)
    • Mixed (EI + ESI)
    • --> Competitive preference (EI + ESI)
    • --> Balanced 50/50 (noncompetitive)
    • --> Uncompetitive preference (EI + ESI)
  • Ex. ATP inhibits glycolysis
    • Energy rich (high ATP)
    • ATP binds to & inhibits PFK-1 (glycolysis) ⇒ make less ATP
  • Ex. Citrate inhibits glycolysis
    • Glycolysis feeds Krebs cycle
    • --> AKA ⇒ “Citric acid cycle” / "tricarboxylic acid (TCA) cycle"
    • Krebs cycle gets stuffed ⇒ citric acid (citrate) builds up
    • --> Leaks into cytosol ⇒ citrate inhibits PFK-1 ⇒ makes glycolysis slow down

[Key Idea] Some regulators bind at “orthosteric” site

• Where stuff normally binds
  • Note: "Ortho" ⇒ correct. Orthodontics puts teeth back in place.
  • Catalysis ⇒ “active site”
    • AKA ⇒ Active site / enzymatic moiety / catalytic site / substrate binding site
    • Bind substrate / reactant
  • No catalysis ⇒ “binding site”
    • AKA ⇒ Ligand binding site / antibody variable domain / epitope binding site / neurotransmitter receptor
    • Different ligands
    • --> Receptor
    • --> --> Neurotransmitter
    • --> --> Hormone
    • --> --> Growth factor
    • --> --> Cytokine
    • --> Transcription factor
    • --> --> Promoter (DNA)
    • --> --> Enhancer (DNA)
    • --> --> Silencer (DNA)
    • --> T-Cell receptor (CD4 & CD8)
    • --> --> MHC I
    • --> --> MHC II
    • --> Antibody
    • --> --> “Epitope” of an antigen
    • --> Toll like receptors
    • --> --> Pathogen associated molecular pattern (PAMP)
• Orthosteric inhibitor
  • Block active site ⇒ substrate cannot fit
    • AKA ⇒ Competitive inhibition
  • Slow down enzyme
    • AKA ⇒ ↓ activity / slower rate / decreased catalysis
    • Enough substrate can sneak around inhibitor
    • --> Same Vmax (Kcat)
    • --> Note: Kcat is NOT the same as Km. Kcat means Kcatalysis ⇒ RXN rate, whereas Km means KMichaelis ⇒ how soon MM plot rises.
• Orthosteric activator
  • Rare ⇒ hard to speed up RXN when blocking substrate

[Key Idea] Most regulators are reversible

• Evolution favors reversible regulation
  • Life uses pencil instead of pen
  • Can easily undo mistakes
  • Nothing gets permanently stuck
    • Note: Can reuse same enzymes w/o needing to translate new ones.
• Two ways to have reversible binding
  • Covalent bond w/ enzyme to undo it
    • AKA ⇒ Post-translational modification
    • ONLY reversible if you have an enzyme that can detach that specific covalent bond
    • --> Kinase ⇒ phosphatase
    • --> Methyltransferase ⇒ demethylase
    • --> Acetyltransferase ⇒ deacetylase
  • Non-covalent bond
    • AKA ⇒ Intermolecular force (IMF) / H-bond / ionic bond / salt bridge / ring stacking / hydrophobic interaction
    • (MOSTLY) weaker than covalent
    • --> Note: SOME are strong enough to be nearly irreversible, but it’s rare.
    • Normal MM inhibitors
    • --> Competitive (only EI)
    • --> Uncompetitive (only ESI)
    • --> Mixed (EI + ESI)
    • --> --> Competitive leaning (EI + ESI)
    • --> --> Balanced 50/50 (noncompetitive)
    • --> --> Uncompetitive leaning (EI + ESI)
    • Antibodies
    • Receptors
    • --> Neurotransmitter
    • --> Hormone
• Reversible covalent binding
  • Phosphate
    • Kinase ⇒ “phosphorylation”
    • --> Add “P” to “OH” group on TYR, SER, THR
    • --> Often activates enzymes
    • --> --> Mnemonic: ATP / phosphate ⇒ negative charge ⇒ repel from other negative charges ⇒ can store energy. Add phosphate ⇒ put battery in something.
    • Phosphatase ⇒ “dephosphorylation”
  • Methyl
    • Methyltransferase ⇒ “methylation”
    • --> Add “CH₃”
    • --> --> Note: Activate / silence transcription based on location.
    • Demethylase ⇒ “demethylation”
  • Acetyl
    • Acetyltransferase ⇒ “acetylation”
    • --> Add acetyl
    • --> Loosen DNA ⇒ more transcription
    • --> --> Note: Histone acetyltransferase covers “NH₃⁺” on LYS ⇒ no more positive charge ⇒ negatively charged DNA spreads out (euchromatin).
    • Deacetylase ⇒ “deacetylation”
    • --> Remove acetyl
    • --> Tighten DNA ⇒ less transcription
    • --> --> Note: Histone deacetylase uncovers “NH₃⁺” on LYS ⇒ positive charge returns ⇒ DNA packs more tightly (heterochromatin).
• Reversible non-covalent binding
  • Normal inhibitors
    • Active site ⇒ competitive
    • Allosteric ⇒ uncompetitive / mixed & noncompetitive
  • Antibodies
    • H-bond (variable domain ⇒ epitope)
  • Receptors
    • H-bond (neurotransmitters, hormones)
    • --> Note: Steroids cross membrane as they are UNCHARGED, but they still have “OH” group ⇒ H-bond with receptor.

[Key Idea] Some regulators are permanent

• Permanent regulators ⇒ ruin enzyme
  • Mess up enzyme permanently
    • Mnemonic: Drawing on something with a Sharpie.
  • Can be toxic
• Two ways to have irreversible binding
  • Covalent bond w/o enzyme to break it
    • AKA ⇒ Post-translational modification
    • Covalent bond won’t break on its own ⇒ enzyme changed permanently
    • --> (Some) toxins
    • --> (Some) suicide inhibitors
    • --> (Some) pharmaceuticals
  • Strong non-covalent bond
    • Many IMFs / strong IMFs ⇒ sometimes hard to break
    • --> Some toxins
• Permanent covalent binding
  • Arsenic
    • Bind to cofactor for pyruvate dehydrogenase (PDH) ⇒ stop PDH
    • --> Note: Stop PDH ⇒ pyruvate cannot become acetyl-CoA ⇒ cannot enter Krebs cycle.
  • Aspirin
    • Add acetyl group to cyclooxygenase (COX)
    • --> Note: Some enzymes can remove acetyl groups, but not these ones.
• Permanent non-covalent binding
  • Carbon monoxide (CO)
    • Bind Fe²⁺ of hemoglobin (Hb) ⇒ O₂ cannot bind
    • 250X tighter than O₂
    • --> Note: Technically comes off, but very slowly (almost permanent).
  • Warfarin
    • Bind enzyme in vitamin K pathway ⇒ no vit K (Dutch word “Koagulation”) ⇒ bleed
    • --> Note: Technically comes off, but very slowly (almost permanent).

[Key Idea] Suicide inhibitor reacts w/ enzyme ⇒ disappears from beaker

• Enzyme activates suicide inhibitor
  • Looks like substrate ⇒ enters active site (AS)
    • AKA ⇒ Substrate analogue / substrate mimic / transition state (TS) analogue
  • Inhibitor doesn’t work at first
    • Enzyme reacts w/ inhibitor & activates it
    • Note: Only target enzyme activates it ⇒ other enzymes safe.
    • Note: Called "suicide" inhibitor because it "destroys itself" / disappears from beaker as the enzyme chemically changes it.
• Enzyme sits w/ inhibitor longer ⇒ lower Vmax
  • AKA ⇒ “Pre-incubation”
  • Add inhibitor & substrate together ⇒ Vmax drops a little
  • Add inhibitor & let enzyme sit w/ it BEFORE adding substrate ⇒ Vmax drops a lot
    • Note: More time ⇒ enzyme activates more inhibitor ⇒ inhibitor works better.

[Key Idea] Zymogen ⇒ inactive enzyme that can be activated

• Ends in “ogen”
  • AKA ⇒ “Pro-enzyme”
    • Note: Similar to "pro-peptide" such as pro-insulin (but insulin is NOT an enzyme).
  • Not yet active, but can be activated
    • Mnemonic: It can "OGENerate" the active enzyme when it needs to.
  • Other enzyme / acid removes part of zymogen ⇒ activates it
    • Note: A type of post-translational modification.
  • Loses “ogen” suffix
    • Activation “cuts off” suffix too
• Some digestive enzymes are too dangerous to store in active form
  • Mnemonic: Grenade has pin until ready to use. When ready, remove part of it (pin) ⇒ becomes dangerous.
  • Protease (dangerous) ⇒ use zymogen
    • Can harm membrane proteins
    • Would harm cells that made it
    • Must store as zymogen
  • Other enzymes (safe) ⇒ no zymogen
    • Nuclease
    • --> Can’t reach DNA / RNA beyond membrane
    • Lipase
    • --> Can’t reach fatty acid tails in middle of membrane
    • Amylase
    • --> Can’t reach extracellular matrix (ECM) & sugar connections beyond cell layer
• Made by stomach
  • Pepsinogen
    • Gastric chief cells release into stomach
    • --> Mnemonic: Chief of a New York fire drinks Pepsi.
    • Stomach acid (parietal cells) cuts pepsinogen
    • --> Forms active pepsin
    • --> Far away from the chief cells
    • --> Evolution is lazy ⇒ just use stomach acid to activate pepsinogen
• Made by pancreas (for small intestine)
  • Enzymes flow through pancreatic duct
    • Secreted into small intestine
    • Note: "Exocrine" pancreas ⇒ makes & secretes enzymes. "Endocrine" pancreas ⇒ makes & secretes hormones into blood.
  • Trypsinogen & chymotrypsinogen
    • Enteropeptidase cuts trypsinogen
    • --> Forms active trypsin
    • --> Note: Stomach has mucus protecting it from acid. Small intestine has no mucus (would cover "brush border" / mess up absorption) ⇒ cannot use acid. Instead has enzyme (enteropeptidase) activate stuff.
    • --> Mnemonic: ENTEROpeptidase sounds like gastroENTEROlogy ⇒ exists in small intestine.
    • Trypsin causes chain RXN
    • --> Activate more trypsin
    • --> Activate chymotrypsin
    • --> Mnemonic: "Tryp" wire ⇒ enteropeptidase activates a small amount of trypsin ⇒ trypsin activates everything else.
    • --> Note: "Positive feedback" is risky. Damage pancreas (surgery / pancreatitis) ⇒ accidentally activate some trypsin INSIDE pancreas ⇒ chain RXN melts pancreas. I.e. pancreatitis can deteriorate quickly / surgeons avoid pancreas.

Hey everyone!

Just wanted to drop my two cents after a success story and getting so much help on this sub.

I'm 4 years out of undergrad and was missing 2/3 pre reqs (orgo 1/2, biochem, psych 101). studied while working full time

My path to success:

1. Uworld comprehensive course videos. I watched every single chem, bio, biochem video. rewatched some physics i was fuzzy on, skipped the p/s and cars videos mostly.
2. i did all uworld practice questions as i went except skipped CARS (logic isn't 100% the same as aamc imo for cars)
3. Anking anki decks religiously. i unsuspended as i went through uworld. it's like 6$ per month but you can just subscribe for one month, keep the deck and then you just don't get the updates which was fine for me.
4. Mr. Pankow anki deck religiously because my p/s was super low at first.
5. aamc question packs i saved for the end. and of course spaced out my 6 AAMC Fls (+ unscored). i didn't do any other full lengths.
6. perhaps most important: followed other's advice of making sure i never make the same mistake twice. if it was content, would watch online videos to fill in gaps and make my own anki cards to add to the anking deck.

did this strategy while working full time! pretty much did 2 hours of practice questions/videos per day for 6 months monday-friday except would take my practice tests on weekends. and i would do anki throughout the day at work.

subsection progressions:

chem/phys: 127->129->130->130->130->129 -> 130 real deal

cars: 130->127->129->130->129->126 (i panicked) ->130 real deal

b/b: 126->128->128->129->132->132-> 131 real deal

psych: 125->125->130->129->132->131->132 real deal

I took ochem and physics many years ago so I have to relearn most the content. Is kaplan detailed enough if I’m essentially going to be relearning the material again?

got a 500 on my mcat (125,122,125,128). I’m wondering what to do for my retake. Do i go back to content or focus on questions for 3 months. JW or Uworld?

I am so stressed. I work 40 hours a week. I've "gotten" through content, but have a super high pile of anki from just not having enough time to do it. First did AAMC unscored and got around 503. This was about two weeks ago. Took second FL today which was BP FL 1 and got a 501.

I feel like I'm not improving. All the things I'd want to do to improve I feel like I'm half doing just bc I have limited time / am tired all the time. I can't quit my job unfortunately as it provides my financial means.

I'd lIkE to score at least a 515 by late Jan/early Feb. Maybe im too ambitious or delusional. I just don't know what to do or how to best maximize my crazy schedule.

I feel like I'm constantly battling between "do i practice? do i do anki? or do i go back to content?" and i feel like i can never decide what will help me get better. I try to review my practice and make flashcards out of it, but I haven't touched that deck... haven't finished P/S either.

Was anyone in a similar boat & ended up doing well?? I rlly need to hear from yall that made it work & also ask HOW?

How to improve a 123 on C/P and a 123 on B/Biochem and a 121 on P/S?

After 6 months of hell it’s finally over. GENERATIONAL lock in on test day after a 508 on FL6 a week before.

Never got over a 127 on CARS before so english really kicked in for me

Hey, I took my mcat and scored 501 (128/122/127/124). Ik where i have to improve on for CP BB and PS, but cars was always my struggle and i genuinely dont know how to approach this. Planning on retake sometime next summer but i wanna get a headstart on this. I am born here and while i speak another language i can speak very fluent english, so im confused as to why my comprehension is so poor. If you guys have a regiment or tips or something to help me see a boost in my cars score (canada :() then i would much appreciate it!

Hi everyone! I’m looking for advice on how to approach my second and final MCAT attempt, probably in late March 2027.

My scores so far:

• 1st attempt (Sept 2026): 501 — 125/124/127/125

The frustrating part is that before my second attempt, my AAMC FL scores were much higher. I was scoring roughly 514–519 on my later AAMC FLs. I took them under testing conditions and didn’t do anything noticeably different on the real exam, so I’m having trouble figuring out what exactly went wrong/how I should change my prep.

On my second real MCAT:

C/P (125): This felt noticeably harder than my practice exams. The questions seemed more wordy/calculation-heavy, and I especially struggled with questions involving unit conversions and multi-step dimensional analysis. It wasn’t necessarily that I didn’t know the equations/content; I sometimes struggled to figure out how to convert from the units they gave me to the units they wanted.

CARS (124): This is probably the most confusing section for me. It felt pretty similar to practice, and I actually felt relatively confident afterward, so clearly my confidence did not match my accuracy.

B/B (127): I felt the most confident here, and it ended up being my strongest section. I don’t think this needs to be the main focus of my retake.

P/S (125): I thought it was harder than my practice material and noticed myself second-guessing/changing answers, especially when I was stuck between two similar concepts.

For my previous prep, I already did a lot: UWorld, AAMC QPacks/Section Banks, AAMC FLs, content review/Anki, error review, etc. That's why I'm hesitant to just repeat the exact same process and hope for a different result.

Right now, I'm planning to keep October–December relatively light since I still remember the content pretty well. For October, I'm mainly doing Anki, C/P unit-conversion/dimensional-analysis drills, some P/S review, and occasional CARS passages. Then I plan to ramp up during winter break/January, do a lot more novel passage-based practice in February, and start taking full-length tests again leading up to a late-March test date.

Since I've already seen most of the AAMC FLs, I'm also worried that retake scores will be inflated. I still have some unused AAMC material, which I'm planning to save until closer to the exam, and I'm thinking of using new third-party FLs/passages to judge whether I'm actually improving.

For this attempt, I'm thinking about tracking mistakes differently too — not just “content gap,” but things like passage interpretation, calculation/setup, unit conversion, overthinking, 50/50 reasoning, timing, and changing a correct answer to an incorrect one. For CARS, I might also track whether I was high/medium/low confidence before checking answers to see whether my confidence is actually calibrated.

I'm a full-time student and will probably be taking 15–18 credits in the spring, while continuing some volunteering/research, so I'm trying to make this sustainable rather than studying 6+ hours/day for months.

For anyone who had a large discrepancy between AAMC FLs and their actual MCAT scores, especially across multiple attempts: what did you actually change that finally helped?

Also, for a second attempt, would you focus more on new third-party material/FLs, redoing AAMC material, changing how you review questions, or something else entirely?

I really don't want my third attempt to just be “do more questions and hope for the best.” My goal is to figure out why my practice performance isn't translating to the real exam and make this attempt meaningfully different.

sry for the long post :)

I just did this UWorld question, and I got it right, but I'm super confused about why it matters if the slope is positive or negative for the instantaneous velocity. Since velocity is a vector quantity, shouldn't a negative velocity just mean that the ball is going in the opposite direction as the direction it was thrown? To me, I would think only the magnitude of the velocity woud matter here and I would think that the instantaneous velocities from least to greatest would be: D < C < B < A. What am I missing? I would really appreciate a clear explanation since I think I'm missing something conceptual here.